I. Kameshita, M. Tokushige, K. Izui
Jun 6, 1977
Citations
0
Influential Citations
3
Citations
Journal
Biochemical and biophysical research communications
Abstract
Abstract Chemical modification of phosphoenolpyruvate carboxylase [EC 4.1.1.31] of Escherichia coli W with 2,3-butanedione, an arginyl residue reagent, results in an inactivation of the enzyme. The inactivation proceeds following pseudo-first order kinetics. DL-Phospholactate, a substrate analog, effectively protects the enzyme from the inactivation. The enzyme modified in the presence of DL-phospholactate or in its absence is completely desensitized to fructose 1,6-bisphosphate and GTP, allosteric activators for the enzyme. At the same time, the sensitivities to acetyl coenzyme a, laurate and L-aspartate are considerably decreased. Resensitization is attained, however, upon removal of excess butanedione and borate by gel filtration, concomitant with the restoration of the catalytic activity.